Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.1.1.27 (lactate dehydrogenase)
 29,211 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Various enzymes of glycolysis (hexokinase, phosphoglucoisomerase, aldolase and lactate dehydrogenase), the Krebs cycle (isocitrate, succinic and malate dehydrogenases), and the pentose phosphate cycle (glucose-6-phosphate and 6-phosphogluconate dehydrogenases) were studied in buffalo spermatozoa by biochemical and cytochemical methods. The enzymes of glycolysis were found to be loosely bound whereas those of the Krebs and pentose phosphate cycles were strongly bound to mitochondrial membranes. All the enzymes studied were localized histochemically in the mid-piece.
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PMID:Glycolytic, Krebs cycle and pentose phosphate cycle enzymes in spermatozoa of the buffalo (Bubalus bubalis). 51 3

Activities of lactate dehydrogenase, glucose-6-phosphate dehydrogenase, transketolase and creatine phosphokinase were studied in tissue of aneurysm and in extrainfarctional part of rat heart muscle after experimental infarction. Activity of total LDH, content of its anode isoenzymes and creatine phosphokinase activity were decreased. Enzymes of pentose phosphate pathway were activated and amount of cathode LDH isoenzymes was increased. The most distinct and apparently irreversible alterations in the enzymatic activity were observed in the aneurysm tissues.
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PMID:[Enzyme activity in post-infarct aneurysm and in the myocardial zone outside the infarct in experimental infarct in rats]. 66 66

1. Measurements have been made of the activities of enzymes of the glycolytic route, the pentose phosphate pathway, the tricarboxylic acid cycle and lipogenesis in liver and adipose tissue from genetically obese (fa/fa) rats and their lean litter mates (fa/ --). The effect of food restriction for a period of three weeks on the enzyme profile of liver and adipose tissue of the obese rat was also studied. 2. The most striking increases in enzyme activity in livers from obese rats were: (a) among enzymes of lipogenesis; ATP-citrate lyase, acetyl-CoA carboxylase, fatty acid synthetase, malate dehydrogenase (decarboxylating) and cytoplasmic glycerolphosphate dehydrogenase; (b) within the pentose phosphate pathway; glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase; (c) within the glycolytic pathway; glucokinase, pyruvate kinase and lactate dehydrogenase. All of these enzymes showed a significant increase in activity on the basis of U/g liver and U/mg DNA. In adipose tissue all the enzymes of lipogenesis, of the glycolytic route, of the oxidative segment of the pentose phosphate pathway and of the tricarboxylic acid cycle were increased when expressed as U/2 fat pads or as U/mg DNA. 3. The restriction of the food intake of obese rats to that consumed by their lean litter mates for periods of three weeks did not produce the expected adaptive decrease in enzymes of lipogenesis; in adipose tissue, only ATP-citrate lyase and malate dehydrogenase (decarboxylating) showed a marked decrease; no significant change was found in adipose tissue or liver of the activities of acetyl-CoA carboxylase and fatty acid synthetase, when expressed on a cell basis (U/mg DNA). The non-oxidative enzymes of the pentose phosphate pathway and enzymes involved in glycerogenesis (pyruvate carboxylase, malate dehydrogenase and phosphoenolpyruvate carboxykinase) all increased in adipose tissue from limit-fed obese rats. 4. The rate of conversion of specifically labelled glucose to (14C)O2 and 14C-labelled lipid by pieces of adipose tissue and by liver slices was also measured. Insulin caused an increase in the conversion of (1-14C)glucose to (14C)O2 and 14C-labelled lipid in obese rats fed ad libitum, limit-fed rats and in their lean litter mates. 5. The results are discussed in relation to the raised insulin and hypothyroid state of the obese rat. The effect of this altered hormonal status on the activity of cyclic nucleotide phosphodiesterases and cellular levels of adenosine 3' :5'-monophosphate and guanosine 3' :5'-monophosphate and guanosine 3' :5'-monophosphate in relation to the obese syndrome is considered.
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PMID:Adaptive responses of enzymes of carbohydrate and lipid metabolism to dietary alteration in genetically obese Zucker rats (fa/fa). 71 Mar 95

Setaria cervi, the filarial parasite inhabiting the Indian water buffalo (Bubalus bubalis Linn.) contained almost all the enzymes involved in glycogen degradation. Significant activities of glycogen phosphorylase, glucokinase, phosphoglucomutase, phosphoglucose isomerase, phosphofructokinase, FDP-aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphopyruvate hydratase, pyruvate kinase, lactate dehydrogenase glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase were detected in cell-free extracts of whole worms. The presence of PEP-carboxykinase, malate dehydrogenase, fumarase and fumarate reductase revealed the functioning of the PEP-succinate pathway in addition to phosphorylating glycolysis and pentose phosphate pathway in the parasite. Excepting fumarate reductase all other enzymes were localized in the particulate-free cytosol fraction, although small amounts of glycogen phosphorylase, aldolase and lactate dehydrogenase were also detected in the mitochondrial fraction.
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PMID:Setaria cervi: enzymes of glycolysis and PEP-succinate pathway. 86 May 72

The lactate and pyruvate levels, as well as acid and alkaline phosphatase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase, glutaminic acid-oxalacetic acid transaminase and aldolase levels of rat liver homogenizates were measured at 24 degrees C and 38 degrees C during 120 min ischaemia from 0 to the 120th min. With the exception of transaminase and aldolase, the other enzymes were also enzyme-histochemically studied. The early lesions of the liver can be detected, both the quantitative laboratory tests and enzyme histochemical studies. The deviations from normal, observed at 24 degrees C between the 60th and 100th min, and at 38 degrees C between the 30th and 60th min, might be signs of irreversible lesions. Fractionated study of the liver homogenizate improves the assessability of enzyme determinations. In the course of "warm" ischaemia, the liver lysosomal lesions are early symptoms. Parallel to the breakdown of aerobic glycolysis lactic acid, fermentation, and an active pentose phosphate cycle can be detected. Quantitative testing of the liver homogenizate and enzyme histochemical observation of the hepatic tissue, might be a suitable method for the assessment of ischaemic liver lesions.
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PMID:Effect of ischaemia on the enzyme activity of the hepatic tissue. 89 61

In soluble fraction of rat liver studies have been made on the activity of glycolytic enzymes and dehydrogenases of the pentose phosphate pathway 3 and 20 hours after the electrical stimulation of the medial (HVM) and lateral (AHL) structures of the medial hypothalamus via chronically implanted electrodes. Electrical stimulation of the HVM within 3 hours decreased total hexokinase, glucose-6-phosphate dehydrogenase, and lactate dehydrogenase activities, and to a lower extent -- the activity of glucokinase. This effect was not prevented by the adrenalectomy. During stimulation of the AHL, the decrease of LDH activity was the same, whereas the activity of hexokinase, glucose-6-phosphate dehydrogenase and glucokinase decreased to a lower extent. Electrical stimulation of the medial hypothalamus within 20 hours decreased the response, this effect being presumably associated with the decrease in the content of endogenous noradrenalin in the liver of animals. The role of the hypothalamus and sympathetic nervous system in regulation of the investigated enzymes of energy metabolism in the liver is discussed.
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PMID:[Participation of the hypothalamus in regulating the activity of rat liver energy metabolism enzymes]. 98 65

Three enzymes selected as representative of major metabolic pathways (malic dehydrogenase, of the citric acid cycle, lactic dehydrogenase, of glycolysis and glucose-6-phosphate dehydrogenase, of the pentose pathway) were measured by quantitative histochemical methods in individual hypothalamic nuclei during the 5-day estrous cycle of adult rats. Malic dehydrogenase increases significantly from low proestrous levels to a peak at estrus and then declines during diestrus in the following nuclei and areas of the anterior hypothalamus: medial and lateral preoptic, suprachiasmatic, supraoptic, and anterior. Significant peaks of lactic dehydrogenase occur more often during diestrus-3 in hypothalamic nuclei of the middle and posterior hypothalamus, Glucose-6-phosphate dehydrogenase has a biphasic pattern with peaks usually occurring during the diestrous period.
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PMID:Quantitative histochemical studies of the hypothalamus. Dehydrogenase enzymes during the estrous cycle. 103 42

The activity of glucose-6-phosphate dehydrogenase, phosphogluconate dehydrogenase, pyruvate kinase (PK) and lactate dehydrogenase (LDH) was measured in human adipose tissue (AT) of newborns aged 0-2 and 2-48 h, of 3- to 5-month-old infants and of adults. AT was sampled by means of a special needle from the gluteal region without anesthesia. We observed significantly higher activity of the two pentose phosphate shunt enzymes when calculated on protein content and wet weight basis in newborns as compared to infants and adults. There were no differences for PK and LDH between newborns and adults when the values were calculated for the soluble protein. The protein concentration of the AT decreased significantly during the development.
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PMID:Activity of some enzymes of carbohydrate metabolism in human subcutaneous adipose tissue in newborns, infants and adults. I. Activity of pyruvate kinase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase. 114 54

Morphological and cytochemical studies on the squirrel monkey have been made after maintaining the sujects on pure distilled water and fluoridated distilled water for 18 months with the objective of determining the effect of fluoride on the activity of some hydrolytic and oxidative enzymes in the kidney, liver and nervous system. Daily water intake by individual animals was measured over the final 10 months of the animal's exposure to 0,1 and 5 ppm fluoride. Water consumption was considerably higher in the animals on higher fluoride intake. Whereas the nervous system remained totally unaffected by this experimental procedure, the liver showed a slightly enhanced acivity of Krebs citric acid cycle enzymes. The kidneys, however, showed significant cytochemical changes, especially in the animals on 5 ppm fluoride intake in their drinking water. In these animals, the glomeruli showed an increase in the activity of acid phosphatase and the enzymes belonging to the citric acid cycle and the pentose shunt, whereas lactate dehydrogenase, a resentative of the anaerobic glyoclytic pathway, remained unchanged or only slightly changed. These observations suggest that fluoride in concentrations as low as 5 ppm interferes to some extent with the intracellular metabolism of the excretory system.
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PMID:Cytochemical response of kidney, liver and nervous system of fluoride ions in drinking water. 115 Apr 82

In the subcommissural organ (SCO) of the guinea pig, rat, golden hamster, and mouse the activity and distribution of enzymes related to the energy-supplying metabolism and of some marker enzymes of different cell organelles have been investigated by means of mostly modified histochemical methods. The results were compared with findings in the ciliated ependyma of the ventricular wall and with those in the ependyma of the choroid plexus of the third ventricle. In the ependymal part of the SCO only a moderate activity of hexokinase is observed in its specialized columnar cells whereas a high activity is present both in the ciliated ependyma and the choroid plexus. - The staining pattern of glucose-6-phosphatase is similar to that of hexokinase but this enzyme is found is the SCO only. - Likewise hexokinase, glycogen granules and enzymes related to glycogen metabolism (phosphoglucomutase, uridine-diphosphoglucose pyrophosphorylase, glycogen synthetase and phosphorylase) are regularly found most numerous and active in the nuclear and supra-nuclear area of the ependymal part. These enzymes are less active in both the other ependymal regions. - Uridine-diphosphoglucose dehydrogenase could not be demonstrated in the SCO. The NADP-linked enzymes of the pentose phosphate shunt, glucose-6-phosphate and 6-phosphogluconate dehydrogenase, show a moderate activity which decreases also from the nuclear towards the apical area of the ependymal cells of the SCO. Enzymes of the glycolytic pathway, such as glucosephosphate isomerase, fructose-6-phosphate kinase, fructose-I,6-diphosphate aldolase, glyceraldehyde-3-phosphate and lactate dehydrogenase, are highly active in the SCO and are located mainly in the supranuclear area, too. Fructose-1,6-diphosphatase could not be demonstrated thus indicating that in the SCO the pathway is most probably only glycolytic but not gluconeogenetic. Compared to the ependyma of the ventricular wall and of the choroid plexus, in the SCO the M type subunits of lactate dehydrogenase predominate. Glycolytic enzymes are also very active in the choroid plexus but less in the ciliated ependyma. Compared to the ciliated ependyma and especially to the ependyma of the choroid plexus, the activities of enzymes which are only present in mitochondria (NAD-linked isocitrate dehydrogenase, succinate dehydrogenase, NAD-linked malate dehydrogenase after preextraction, cytochrome oxidase, 3-hydroxybutyrate and glycerolphosphate and glutamate dehydrogenase) are relatively low. Mitochondria are accumulated near the superior pole of the nuclei as well as in the most apical part of the ependymal cells. - The staining pattern of NADP-linked isocitrate and malate dehydrogenase as well as of NADH dehydrogenase suggests that these enzymes are localized both in and out of mitochondria. The extramitochondrial activity of the first two enzymes might be localized in the cytosol. The extramitochondrial activity of NADH dehydrogenase might be localized in the endoplasmic reticulum...
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PMID:Enzymatic organization of the subcommissural organ. 123 49


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